› 5hi8

X-ray diffraction
1.8Å resolution

Structure of T-type Phycobiliprotein Lyase CpeT from Prochlorococcus phage P-HM1

Released:
DOI: 10.2210/pdb5hi8/pdb
PDB entry 5hi8 coloured by chain, front view.
PDB entry 5hi8 coloured by chain, side view.
PDB entry 5hi8 coloured by chain, top view.
Source organism: Prochlorococcus phage P-HM1
Primary publication:
Distinct Features of Cyanophage-encoded T-type Phycobiliprotein Lyase ΦCpeT: THE ROLE OF AUXILIARY METABOLIC GENES.
Gasper R, Schwach J, Hartmann J, Holtkamp A, Wiethaus J, Riedel N, Hofmann E, Frankenberg-Dinkel N
J Biol Chem 292 3089-3098 (2017)
PMID: 28073912

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-122907 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Antenna protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 136 amino acids
Theoretical weight: 16.29 KDa
Source organism: Prochlorococcus phage P-HM1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: E3SMK9 (Residues: 1-134; Coverage: 100%)
Gene names: PHM1_028, cpeT
Sequence domains: CpeT/CpcT family (DUF1001)

Ligands and Environments

2 bound ligands:
Ligand MG 2 x MG
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: C2
Unit cell:
a: 63.29Å b: 61.68Å c: 93.34Å
α: 90° β: 109.77° γ: 90°
R-values:
R R work R free
0.208 0.207 0.228
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 citation in other articles

Distinct molecular signatures in dissolved organic matter produced by viral lysis of marine cyanobacteria.
Ma et al. (2018)
7 more

4 mentions without citation

A Review on Viral Metagenomics in Extreme Environments.
Dávila-Ramos et al. (2019)
3 more